Cellular folate deficiency induces a number of homeostatic physiological changes to restore cellular folate levels, including the upregulation of folate receptor levels. An initial consequence of folate deficiency is an increase in intracellular homocysteine levels that results in the homocysteinylation of the multifunctional heterogeneous nuclear ribonucleoprotein protein-E1 (hnRNP-E1). Homocysteinylation of hnRNP-E1 forms cysteine-S-S mixed disulfide bonds, which unmasks a cryptic mRNA-binding site that is capable of binding to diverse mRNAs characterized as having a common poly(rC)/poly(U)-rich cis element. Binding of homocysteinylated hnRNP-E1 to poly(rC)/(U)-containing mRNAs, including the folate receptor-alpha (folate receptor-α) mRNA, leads to an increase in translation on the mRNAs and a net increase in their corresponding protein levels. Thus, the capability to control the binding of hnRNP-E1 to the poly(rC)/(U)-containing mRNAs independent of homocystein may be useful to alter the expression of a subset of proteins for the treatment of a number of health conditions.